Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides

The aim of the study presented here was to determine if there is a correlation between the presence of specific protein domains within tree nut allergens or tree nut allergen epitopes and the frequency of bioactive fragments and the predicted susceptibility to enzymatic digestion in allergenic prote...

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Main Authors: Piotr Minkiewicz, Christopher P. Mattison, Małgorzata Darewicz
Format: Article
Language:English
Published: MDPI AG 2022-07-01
Series:Current Issues in Molecular Biology
Subjects:
Online Access:https://www.mdpi.com/1467-3045/44/7/214
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author Piotr Minkiewicz
Christopher P. Mattison
Małgorzata Darewicz
author_facet Piotr Minkiewicz
Christopher P. Mattison
Małgorzata Darewicz
author_sort Piotr Minkiewicz
collection DOAJ
description The aim of the study presented here was to determine if there is a correlation between the presence of specific protein domains within tree nut allergens or tree nut allergen epitopes and the frequency of bioactive fragments and the predicted susceptibility to enzymatic digestion in allergenic proteins from tree nuts of cashew (<i>Anacardium occidentale</i>), pecan (<i>Carya illinoinensis</i>), English walnut (<i>Juglans regia</i>) and pistachio (<i>Pistacia vera</i>) plants. These bioactive peptides are distributed along the length of the protein and are not enriched in IgE epitope sequences. Classification of proteins as bioactive peptide precursors based on the presence of specific protein domains may be a promising approach. Proteins possessing a vicilin, N-terminal family domain, or napin domain contain a relatively low occurrence of bioactive fragments. In contrast, proteins possessing the cupin 1 domain without the vicilin N-terminal family domain contain a relatively high total frequency of bioactive fragments and predicted release of bioactive fragments by the joint action of pepsin, trypsin, and chymotrypsin. This approach could be utilized in food science to simplify the selection of protein domains enriched for bioactive peptides.
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spelling doaj.art-95aeae8022af4be08fcaaad86744f7aa2023-11-23T12:36:08ZengMDPI AGCurrent Issues in Molecular Biology1467-30371467-30452022-07-014473100311710.3390/cimb44070214Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive PeptidesPiotr Minkiewicz0Christopher P. Mattison1Małgorzata Darewicz2Chair of Food Biochemistry, University of Warmia and Mazury in Olsztyn, Plac Cieszyński 1, 10-726 Olsztyn-Kortowo, PolandSouthern Regional Research Center, FPSQ, ARS, U.S. Department of Agriculture, New Orleans, LA 70124, USAChair of Food Biochemistry, University of Warmia and Mazury in Olsztyn, Plac Cieszyński 1, 10-726 Olsztyn-Kortowo, PolandThe aim of the study presented here was to determine if there is a correlation between the presence of specific protein domains within tree nut allergens or tree nut allergen epitopes and the frequency of bioactive fragments and the predicted susceptibility to enzymatic digestion in allergenic proteins from tree nuts of cashew (<i>Anacardium occidentale</i>), pecan (<i>Carya illinoinensis</i>), English walnut (<i>Juglans regia</i>) and pistachio (<i>Pistacia vera</i>) plants. These bioactive peptides are distributed along the length of the protein and are not enriched in IgE epitope sequences. Classification of proteins as bioactive peptide precursors based on the presence of specific protein domains may be a promising approach. Proteins possessing a vicilin, N-terminal family domain, or napin domain contain a relatively low occurrence of bioactive fragments. In contrast, proteins possessing the cupin 1 domain without the vicilin N-terminal family domain contain a relatively high total frequency of bioactive fragments and predicted release of bioactive fragments by the joint action of pepsin, trypsin, and chymotrypsin. This approach could be utilized in food science to simplify the selection of protein domains enriched for bioactive peptides.https://www.mdpi.com/1467-3045/44/7/214food allergytree nutbioactivepeptidebioinformaticscupin
spellingShingle Piotr Minkiewicz
Christopher P. Mattison
Małgorzata Darewicz
Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides
Current Issues in Molecular Biology
food allergy
tree nut
bioactive
peptide
bioinformatics
cupin
title Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides
title_full Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides
title_fullStr Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides
title_full_unstemmed Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides
title_short Quantitative In Silico Evaluation of Allergenic Proteins from <i>Anacardium occidentale</i>, <i>Carya illinoinensis</i>, <i>Juglans regia</i> and <i>Pistacia vera</i> and Their Epitopes as Precursors of Bioactive Peptides
title_sort quantitative in silico evaluation of allergenic proteins from i anacardium occidentale i i carya illinoinensis i i juglans regia i and i pistacia vera i and their epitopes as precursors of bioactive peptides
topic food allergy
tree nut
bioactive
peptide
bioinformatics
cupin
url https://www.mdpi.com/1467-3045/44/7/214
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AT christopherpmattison quantitativeinsilicoevaluationofallergenicproteinsfromianacardiumoccidentaleiicaryaillinoinensisiijuglansregiaiandipistaciaveraiandtheirepitopesasprecursorsofbioactivepeptides
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